Purification of L-[3H]nicotine eliminates low affinity binding

Life Sci. 1990;46(13):935-43. doi: 10.1016/0024-3205(90)90095-9.

Abstract

Some studies of L-[3H]nicotine binding to rodent and human brain tissue have detected two binding sites as evidenced by nonlinear Scatchard plots. Evidence presented here indicates that the low affinity binding site is not stereospecific, is not inhibited by low concentrations of cholinergic agonists and is probably due to breakdown products of nicotine since purification of the L-[3H]nicotine eliminates the low affinity site.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alkaloids / pharmacology
  • Animals
  • Autoradiography
  • Azocines
  • Binding Sites
  • Binding, Competitive
  • Brain / metabolism*
  • Carbachol
  • Chromatography, Thin Layer
  • Ligands
  • Lobeline / pharmacology
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Nicotine / isolation & purification*
  • Nicotine / metabolism
  • Quinolizines

Substances

  • Alkaloids
  • Azocines
  • Ligands
  • Quinolizines
  • cytisine
  • Nicotine
  • Carbachol
  • Lobeline